CATW_FELCA
ID CATW_FELCA Reviewed; 374 AA.
AC Q9TST1;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cathepsin W;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=CTSW;
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphocyte;
RA Kovacs E.M., Robinson W.F.;
RT "FIV infection induces apoptosis and alters host gene expression.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a specific function in the mechanism or regulation
CC of T-cell cytolytic activity. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P56202}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB59816.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ012326; CAB59816.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001116343.1; NM_001122871.1.
DR STRING; 9685.ENSFCAP00000005174; -.
DR MEROPS; C01.037; -.
DR GeneID; 100144390; -.
DR KEGG; fca:100144390; -.
DR CTD; 1521; -.
DR eggNOG; KOG1542; Eukaryota.
DR InParanoid; Q9TST1; -.
DR OrthoDB; 1264766at2759; -.
DR TreeFam; TF337736; -.
DR Proteomes; UP000011712; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02248; Peptidase_C1A; 1.
DR InterPro; IPR033158; Cathepsin_W.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR InterPro; IPR039417; Peptidase_C1A_papain-like.
DR InterPro; IPR013201; Prot_inhib_I29.
DR PANTHER; PTHR12411:SF101; PTHR12411:SF101; 1.
DR Pfam; PF08246; Inhibitor_I29; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR PRINTS; PR00705; PAPAIN.
DR SMART; SM00848; Inhibitor_I29; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Thiol protease; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..127
FT /evidence="ECO:0000255"
FT /id="PRO_0000026325"
FT CHAIN 128..374
FT /note="Cathepsin W"
FT /id="PRO_0000026326"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT ACT_SITE 291
FT /evidence="ECO:0000250"
FT ACT_SITE 329
FT /evidence="ECO:0000250"
FT CARBOHYD 205
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 347
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 150..191
FT /evidence="ECO:0000250"
FT DISULFID 184..226
FT /evidence="ECO:0000250"
SQ SEQUENCE 374 AA; 41644 MW; 12879CCF651CEC98 CRC64;
MAITVYLSCL LVLSMAGLAQ GIKSSLRSQD PGPQPLELKQ AFTLFQIQYN RSYSNPEEYA
RRLDIFAHNL AQAQQLEEED LGTAEFGVTP FSDLTEEEFG RLYGHRRMDG EAPKVGREVG
SEEWGESVPP TCDWRKLDGV ISSVKKQESC SCCWAMAAAG NIEALWAIKY RQSVELSVQE
LLDCGRCGDG CRGGFVWDAF ITVLNNSGLA SEKDYPFQGQ VKPHRCLAKK RTKVAWIQDF
IMLPDNEQKI AWYLATQGPI TVTINMKLLK LYKKGVIEAT PTSCDPFLVD HSVLLVGFGK
SESVADRRAG AAGAQPQSRR SIPFWILKNS WGTKWGXGGY FRLYRGNNTC GITKYPLTAR
VDQPAKKRPV SCPP